The FQH431SNLKQMSEFSVFLSLRNLIYLDISH456TH458TR fragment, containing three histidine residues, the conserved H431 and the non-conserved H456 and H458, located from 429 to 460 amino acid residues in the C-terminal portion of human Toll-like-receptor 4 (hTLR4), which is directly activated by nickel, a well known contact allergen, has been tested for Ni(II) binding. The complex formation capability of the 32-amino acid sequence with Ni(II) ions has been followed by potentiometric, UV-Vis, CD, MS and NMR measurements. Ni(II) is able to bind to all three histidines by forming macrocycle complexes at low and physiological pH. From pH 9 on, a 4N diamagnetic species (N(im), 3N(am)(-)) with the participation of an imidazole nitrogen and three deprotonated nitrogens from His28, Ser27 and Ile26 amides from the backbone of the model peptide has been determined. From the NMR results it was possible to determine that His28, which mimics the H456 residue in the protein, together with the environment around it, was mainly involved in the binding.

Ni(II) binding to 429-460 peptide fragment from human Toll like receptor (hTLR4): a crucial role for nickel-induced contact allergy? / Zoroddu, Maria Antonietta; M., Peana; Medici, Serenella; S., Potocki; H., Kozlowski. - In: DALTON TRANSACTIONS. - ISSN 1477-9226. - 43:(2014), pp. 2764-2771.

Ni(II) binding to 429-460 peptide fragment from human Toll like receptor (hTLR4): a crucial role for nickel-induced contact allergy?

ZORODDU, Maria Antonietta;M. Peana;MEDICI, Serenella;
2014-01-01

Abstract

The FQH431SNLKQMSEFSVFLSLRNLIYLDISH456TH458TR fragment, containing three histidine residues, the conserved H431 and the non-conserved H456 and H458, located from 429 to 460 amino acid residues in the C-terminal portion of human Toll-like-receptor 4 (hTLR4), which is directly activated by nickel, a well known contact allergen, has been tested for Ni(II) binding. The complex formation capability of the 32-amino acid sequence with Ni(II) ions has been followed by potentiometric, UV-Vis, CD, MS and NMR measurements. Ni(II) is able to bind to all three histidines by forming macrocycle complexes at low and physiological pH. From pH 9 on, a 4N diamagnetic species (N(im), 3N(am)(-)) with the participation of an imidazole nitrogen and three deprotonated nitrogens from His28, Ser27 and Ile26 amides from the backbone of the model peptide has been determined. From the NMR results it was possible to determine that His28, which mimics the H456 residue in the protein, together with the environment around it, was mainly involved in the binding.
2014
Ni(II) binding to 429-460 peptide fragment from human Toll like receptor (hTLR4): a crucial role for nickel-induced contact allergy? / Zoroddu, Maria Antonietta; M., Peana; Medici, Serenella; S., Potocki; H., Kozlowski. - In: DALTON TRANSACTIONS. - ISSN 1477-9226. - 43:(2014), pp. 2764-2771.
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11388/59751
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 26
  • ???jsp.display-item.citation.isi??? ND
social impact